Localization of Heparin- and Neuropilin-1-recognition Sites of Viral Vegfs.
From: Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose, Tokyo 204-8588, Japan.
Biochemical and biophysical research communications
- Publish Date: Sep 2006
- ISSN: 0006-291X
- Volume: 348
- Issue: 3
- Pages: 957-62
- Medium: Print
- Language: English
- Citation (JAMA): Tokunaga Yuko, Yamazaki Yasuo, Morita Takashi, et al. Localization of Heparin- and Neuropilin-1-recognition Sites of Viral Vegfs.. Biochem. Biophys. Res. Commun. Sep 2006;348:957-62
Abstract
VEGF-A165 plays a central role in neovascularization. The biological activities of VEGF-A165 are largely mediated through KDR. VEGF-A165 also binds to cellular coreceptors, neuropilin-1 (NP-1), and heparin, via its C-terminal domain, resulting in functional modulation. Parapoxvirus-encoded VEGFs (PV-VEGFs), which recognize KDR, possess basic amino acid clusters in their C-terminal regions. Some PV-VEGFs may interact with NP-1; however, the NP-1- and heparin-binding properties have not been fully characterized. Here, we demonstrate that the heparin- and NP-1-binding region of PV-VEGFs is located in its C-terminal tail. Furthermore, the two arginine residues adjacent to the C-terminus greatly contribute to both interactions.
Mesh Headings (Keywords): Binding Sites, Heparin, Neuropilin-1, Parapoxvirus, Peptide Fragments, Protein Binding, Vascular Endothelial Growth Factors
Check for Full Text / PubMed Unique Identifier (PMID): 16899214
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.